IED ID | IndEnz0001000049 |
Enzyme Type ID | amylase000049 |
Protein Name |
Maltase 2 EC 3.2.1.20 |
Gene Name | Mal-B2 Mav2 GJ22506 |
Organism | Drosophila virilis (Fruit fly) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Drosophila virilis group Drosophila virilis (Fruit fly) |
Enzyme Sequence | MAAAHQLTRTTQLLLLCSLLWTQAPRPVMSSLLSAQTEDFIDWWQHAVFYQIYPRSFKDSNGDGIGDLQGVISKLPYLAETGITATWLSPIFQSPMVDFGYDVSDYKSIQTEYGTMADFEQLVNTATSLGIKIILDFVPNHTSDKHEWFIKSAARDPLYDNFYVWADGKLDNQGVRQPPNNWQSVFYGSAWQWHEQRGQYYLHQFAKEQPDLNFRNPAVVRAMDDVLLFWLNKGVAGFRIDALNHLFEDETLPDEPLSGKTTDPLSYDYTKHIYTKDLPEVLSMVQHWRQLLDDYTAKHSEGATRIMMTEAYADLQVLMDYYEDAGGVRGSQLPFNFHFITDVSGDSDARDFVYNIEKWLIYMPRGHTANWVMGNHDKPRVATRFGPASVDAMNMLLLTLPGVAVTYNGEELGMQDYDEISWEDTVDPPARIAGKLDYKKVSRDPERTPFQWSNATNAGFSTAAKTWLPVNPNYLVLNLEAQKQAVKSHYKVYKSLIELRKLPVLRRGRFSIEPLSRTVFAFKRTLKDYDTLVTIINVSAKEQLVNLTDFINRPQKLVVEVAGVDSVYAPGQTISSSALTLSAHEGLICKLLDA |
Enzyme Length | 594 |
Uniprot Accession Number | O16099 |
Absorption | |
Active Site | ACT_SITE 241; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 310; /note=Proton donor; /evidence=ECO:0000250 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.; EC=3.2.1.20; |
DNA Binding | |
EC Number | 3.2.1.20 |
Enzyme Function | |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Erroneous gene model prediction (1); Glycosylation (4); Sequence conflict (2); Signal peptide (1); Site (1) |
Keywords | Glycoprotein;Glycosidase;Hydrolase;Reference proteome;Signal |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..30; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 67,586 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |